Characterization of intron 7 to exon 8 of heat shock protein 90-aa1 (hsp90aa1) gene in dominant brown layer chicken using some bioinformatic tools

Abstract


 HSP90AA1, an isoform of HSP90 has been characterized to indicate it plays important roles in basic cellular events. It is activated in chicken in response to heat stress. This study was aimed at the computational analysis of the biochemical cum structural features and an evolutionary relationship study on the HSP90AA1 gene in Dominant brown layers (DBL) and some selected avian species using bioinformatics tools. ProtParam for physicochemical properties. Scanprosite for post-translational modification sites, Netphos-3.1 for phosphorylation sites, BDM-PUB program for Ubiquitination sites, PDBSUM for Secondary structure and homology modelling with SWISS-model. The findings revealed that intron 7 and exon 8 of HSP90AA1 protein in DBL had a molecular weight of 24681.19Da and an instability index of 27.60, contains N-myristoylation, Protein-kinase-C-phosphorylation and Tyrosine-kinase-phosphorylation site-2 post-translational modification sites, 4-serine and 2-threonine phosphorylation sites and 12-ubiquitination sites. The evolutionary relationship study found Japanese quail to be in a sister branch close to DBL and chicken. Motifs detected in the avian species revealed the gene to be highly conserved. The secondary structure consisted of 16-helices, 3-sheets and 14-strands. The homology modelling was 87.25% sequence identity with human MC-HSP90-alpha. The study elucidates the components and characteristics of HSP90AA1 in DBL in response to heat stress.